scholarly journals Genetic Alterations and Aberrant Expression of Genes Related to the Phosphatidyl-lnositol-3′-Kinase/Protein Kinase B (Akt) Signal Transduction Pathway in Glioblastomas

2006 ◽  
Vol 13 (4) ◽  
pp. 507-518 ◽  
Author(s):  
Christiane B. Knobbe ◽  
Guido Reifenberger
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Protein Kinase B ◽  
Signal Transduction Pathway ◽  
Genetic Alterations ◽  
Transduction Pathway ◽  
Aberrant Expression ◽  
Expression Of Genes

Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes

1993 ◽  
Vol 13 (9) ◽  
pp. 5659-5669 ◽  
Author(s):  
M Tyers ◽  
B Futcher
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Signal Transduction Pathway ◽  
Mitogen Activated Protein Kinase ◽  
G1 Phase ◽  
Transduction Pathway ◽  
Yeast Saccharomyces Cerevisiae ◽  
Alpha Factor ◽  
Mitogen Activated Protein

In the yeast Saccharomyces cerevisiae, the Cdc28 protein kinase controls commitment to cell division at Start, but no biologically relevant G1-phase substrates have been identified. We have studied the kinase complexes formed between Cdc28 and each of the G1 cyclins Cln1, Cln2, and Cln3. Each complex has a specific array of coprecipitated in vitro substrates. We identify one of these as Far1, a protein required for pheromone-induced arrest at Start. Treatment with alpha-factor induces a preferential association and/or phosphorylation of Far1 by the Cln1, Cln2, and Cln3 kinase complexes. This induced interaction depends upon the Fus3 protein kinase, a mitogen-activated protein kinase homolog that functions near the bottom of the alpha-factor signal transduction pathway. Thus, we trace a path through which a mitogen-activated protein kinase regulates a Cdc2 kinase.

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